DIMT1 Human

DIM1 specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3’-end of 18S rRNA in the 40S ribosomal subunit . This modification is critical for the proper processing of pre-rRNA, leading to the production of small-subunit rRNA independently of its RNA-modifying catalytic activity . DIM1 is part of the small subunit (SSU) processome, which is the first precursor of the small eukaryotic ribosomal subunit .

In humans, DIM1 is localized in the nucleolus, where it performs its function in rRNA processing . The yeast ortholog of this protein functions in the cytoplasm, highlighting a difference in subcellular localization between species .

Recombinant human DIM1 is often expressed in Escherichia coli for research purposes. The recombinant protein is typically purified to a high degree of purity (>90%) and is suitable for various applications such as SDS-PAGE and mass spectrometry . The recombinant form retains the ability to specifically dimethylate the target adenosines in 18S rRNA, making it a valuable tool for studying ribosome biogenesis and function .

DIM1 is a well-studied methyltransferase due to its essential role in ribosome biogenesis. Understanding its function and mechanism can provide insights into the broader processes of RNA modification and ribosome assembly. Additionally, studying the human recombinant form of DIM1 can help elucidate its role in various cellular processes and its potential implications in diseases related to ribosome dysfunction .